The wide use of polyacrylamide gel electrophoresis (“PAGE”) in research, in diagnostics studies, and in biochemistry laboratories in general is due in large part to the optical transparency and electrical neutrality of polyacrylamide gels, as well as the flexibility and adaptability of polyacrylamide gels to a wide range of molecular sizes of the species to be separated in the gel. This flexibility arises from the manufacturer's ability to control the porosity of the gel by varying the concentration of the acrylamide monomer and the proportion of the crosslinking agent, generally bis-acrylamide, relative to the monomer. PAGE is particularly useful for protein separations when sodium dodecyl sulfate (SDS) is incorporated into the gel with an appropriate buffer. Commonly used buffers are tris(hydroxymethyl)aminomethane (“Tris”) and bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane (“Bis-Tris”). Prominent among polyacrylamide gels for protein separations is one originally described by Laemmli, U.K., Nature 227: 680 (1970), which contains Tris-HCl as a buffer at pH 8.8. Unfortunately, the high pH causes these gels to hydrolyze over time, even when the gels are refrigerated. Hydrolysis reduces the migration distance of individual proteins and lowers the resolution of the protein bands. If the pH is lowered in an attempt to avert hydrolysis, the separation of proteins by the gel is less clear and useful analyses of protein mixtures can no longer be obtained.